Expansion and functional diversification of a leucyl aminopeptidase family that encodes the major protein constituents of <it>Drosophila </it>sperm

<p>Abstract</p> <p>Background</p> <p>The evolutionary diversification of gene families through gene creation (and loss) is a dynamic process believed to be critical to the evolution of functional novelty. Previous identification of a closely related family of eight anno...

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Main Authors: Karr Timothy L, Wilkin Elaine C, Dorus Steve
Format: Article
Language:English
Published: BMC 2011-04-01
Series:BMC Genomics
Subjects:
Online Access:http://www.biomedcentral.com/1471-2164/12/177
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spelling doaj-3b34d9c259a445eba8c8946c6e2e5fa52020-11-24T20:42:28ZengBMCBMC Genomics1471-21642011-04-0112117710.1186/1471-2164-12-177Expansion and functional diversification of a leucyl aminopeptidase family that encodes the major protein constituents of <it>Drosophila </it>spermKarr Timothy LWilkin Elaine CDorus Steve<p>Abstract</p> <p>Background</p> <p>The evolutionary diversification of gene families through gene creation (and loss) is a dynamic process believed to be critical to the evolution of functional novelty. Previous identification of a closely related family of eight annotated metalloprotease genes of the M17 Merops family in the <it>Drosophila </it>sperm proteome (termed, Sperm-LeucylAminoPeptidases, S-LAPs 1-8) led us to hypothesize that this gene family may have experienced such a diversification during insect evolution.</p> <p>Results</p> <p>To assess putative functional activities of S-LAPs, we (i) demonstrated that all S-LAPs are specifically expressed in the testis, (ii) confirmed their presence in sperm by two-dimensional gel electrophoresis and mass spectrometry, (iii) determined that they represent a major portion of the total protein in sperm and (iv) identified aminopeptidase enzymatic activity in sperm extracts using LAP-specific substrates. Functionally significant divergence at the canonical M17 active site indicates that the largest phylogenetic group of S-LAPs lost catalytic activity and likely acquired novel, as yet undetermined, functions in sperm prior to the expansion of the gene family.</p> <p>Conclusions</p> <p>Comparative genomic and phylogenetic analyses revealed the dramatic expansion of the S-LAP gene family during <it>Drosophila </it>evolution and copy number heterogeneity in the genomes of related insects. This finding, in conjunction with the loss of catalytic activity and potential neofunctionalization amongst some family members, extends empirical support for pervasive "revolving door" turnover in the evolution of reproductive gene family composition and function.</p> http://www.biomedcentral.com/1471-2164/12/177spermproteomicsgene duplicationgene familyproteasespermatogenesistestis
collection DOAJ
language English
format Article
sources DOAJ
author Karr Timothy L
Wilkin Elaine C
Dorus Steve
spellingShingle Karr Timothy L
Wilkin Elaine C
Dorus Steve
Expansion and functional diversification of a leucyl aminopeptidase family that encodes the major protein constituents of <it>Drosophila </it>sperm
BMC Genomics
sperm
proteomics
gene duplication
gene family
protease
spermatogenesis
testis
author_facet Karr Timothy L
Wilkin Elaine C
Dorus Steve
author_sort Karr Timothy L
title Expansion and functional diversification of a leucyl aminopeptidase family that encodes the major protein constituents of <it>Drosophila </it>sperm
title_short Expansion and functional diversification of a leucyl aminopeptidase family that encodes the major protein constituents of <it>Drosophila </it>sperm
title_full Expansion and functional diversification of a leucyl aminopeptidase family that encodes the major protein constituents of <it>Drosophila </it>sperm
title_fullStr Expansion and functional diversification of a leucyl aminopeptidase family that encodes the major protein constituents of <it>Drosophila </it>sperm
title_full_unstemmed Expansion and functional diversification of a leucyl aminopeptidase family that encodes the major protein constituents of <it>Drosophila </it>sperm
title_sort expansion and functional diversification of a leucyl aminopeptidase family that encodes the major protein constituents of <it>drosophila </it>sperm
publisher BMC
series BMC Genomics
issn 1471-2164
publishDate 2011-04-01
description <p>Abstract</p> <p>Background</p> <p>The evolutionary diversification of gene families through gene creation (and loss) is a dynamic process believed to be critical to the evolution of functional novelty. Previous identification of a closely related family of eight annotated metalloprotease genes of the M17 Merops family in the <it>Drosophila </it>sperm proteome (termed, Sperm-LeucylAminoPeptidases, S-LAPs 1-8) led us to hypothesize that this gene family may have experienced such a diversification during insect evolution.</p> <p>Results</p> <p>To assess putative functional activities of S-LAPs, we (i) demonstrated that all S-LAPs are specifically expressed in the testis, (ii) confirmed their presence in sperm by two-dimensional gel electrophoresis and mass spectrometry, (iii) determined that they represent a major portion of the total protein in sperm and (iv) identified aminopeptidase enzymatic activity in sperm extracts using LAP-specific substrates. Functionally significant divergence at the canonical M17 active site indicates that the largest phylogenetic group of S-LAPs lost catalytic activity and likely acquired novel, as yet undetermined, functions in sperm prior to the expansion of the gene family.</p> <p>Conclusions</p> <p>Comparative genomic and phylogenetic analyses revealed the dramatic expansion of the S-LAP gene family during <it>Drosophila </it>evolution and copy number heterogeneity in the genomes of related insects. This finding, in conjunction with the loss of catalytic activity and potential neofunctionalization amongst some family members, extends empirical support for pervasive "revolving door" turnover in the evolution of reproductive gene family composition and function.</p>
topic sperm
proteomics
gene duplication
gene family
protease
spermatogenesis
testis
url http://www.biomedcentral.com/1471-2164/12/177
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